ID K9ST84_9SYNE Unreviewed; 1787 AA.
AC K9ST84;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Putative extracellular nuclease {ECO:0000313|EMBL:AFY73355.1};
GN ORFNames=Syn7502_01256 {ECO:0000313|EMBL:AFY73355.1};
OS Synechococcus sp. PCC 7502.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY73355.1, ECO:0000313|Proteomes:UP000010385};
RN [1] {ECO:0000313|EMBL:AFY73355.1, ECO:0000313|Proteomes:UP000010385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY73355.1,
RC ECO:0000313|Proteomes:UP000010385};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003594; AFY73355.1; -; Genomic_DNA.
DR STRING; 1173263.Syn7502_01256; -.
DR KEGG; synp:Syn7502_01256; -.
DR PATRIC; fig|1173263.3.peg.1296; -.
DR eggNOG; COG2374; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR eggNOG; COG3391; Bacteria.
DR HOGENOM; CLU_001070_0_0_3; -.
DR OrthoDB; 581389at2; -.
DR Proteomes; UP000010385; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0007154; P:cell communication; IEA:InterPro.
DR CDD; cd10283; MnuA_DNase1-like; 1.
DR CDD; cd04486; YhcR_OBF_like; 1.
DR Gene3D; 2.60.40.2030; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 1.
DR InterPro; IPR038081; CalX-like_sf.
DR InterPro; IPR003644; Calx_beta.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR42834; ENDONUCLEASE/EXONUCLEASE/PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR PANTHER; PTHR42834:SF1; ENDONUCLEASE_EXONUCLEASE_PHOSPHATASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_3G09210); 1.
DR Pfam; PF03160; Calx-beta; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00353; HemolysinCabind; 1.
DR Pfam; PF00932; LTD; 1.
DR SUPFAM; SSF51120; beta-Roll; 1.
DR SUPFAM; SSF141072; CalX-like; 2.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 1.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 1.
DR PROSITE; PS51841; LTD; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000010385};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 312..436
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
SQ SEQUENCE 1787 AA; 185107 MW; F4142A8D9A68EDC6 CRC64;
MATTLSSGDI AFLSLIADNP DTFSFVLLKD IDAGTIINVT DNGFLSSGSL RTGEGVLQYV
AASALTVGTV ITYIDGTSNT NWTNVSGGTS FALSTSGDSL IAFQGTLTGS GSSTTSTNPT
FLAAVTINRS TFDANAADSN TTALPTGLTD GVNAVAVGNT SAEFDNARYT GPTSFASVAE
ARTAINTTSN WTKSNSDTTN FSGTFTIGAV TPTVNLSVSS NAGTEAGTTQ ITVTATASGA
VTGAQTVNLG VTGTGISTGD YNLSNTTITI PDGQTQGSVT FTIVDDAAIE GTETAILTIS
NPSGGITLGN TTTQNIAIAD NESAIQITEY MYNPSSTGGE FVEFTNLGTS TVDFAGWSFD
DNSRTAGSFS LSAFGIVQAG ESVILTESDA AAFRTAWNLP NTVKVIGGLN QNLGRADEIN
VYDASNNLVD RLTYGDQTYA GTIRTQGFSG WTPITNLEPT TINTSWQLSA VNDAQNSQTS
ANGDVGNPGV YNLSAGVNIF QSGGITNITE GGATDTYNVV LRTQPASNVT IAINGGTQTT
NNPSTLTFTS ANWFTPQTVT VSAVDDSVFE GNHTGTITFS TTSSDANYNN ITINSVTANI
TDNDQPGAAP TIQVNTTTTT NFLDGGSLNS LPVSGSGLVS GVINDPTDPA KNFGIDFAIA
DTDTPVGNLT VTVTSNNQSV VTDASLTSNL TGTGATRNLK INPVGVGLAN ITVTVSDGAQ
TSTYIINYAA SAASVNPSTT RFLTGAANAS TAIAIDANYM LVADDENQGL RLYDRQNSGL
PLNSFDFTSS LGLTDLSGGI PREVDIEASA KLGNRIFWLG SESNSDSGNS RPNRDRIFGT
DISGSGANTT LSFAGRYDYL REDIINWDKN NVHGLGANFF GLDASAASGV GSKQSDGYNI
EGLVFAPDNI TAYVSFRAPQ EPTSGRTKAL IVPVTNFTSL LSSNNGGTLG SATFGAPIQL
DLGGRGIREI AKNANNQYVI IAGPAGDATG VPPFDFRLYT WTGNAADTPV LRSANLTALN
SGGSFESIVS VPDNLDSNSQ IQLLVDNGTT DFYNTGLAGS DIPDKPNFQK SRSEIVTIGA
PQVAIHDIQG AAHISPLVGQ NVTGVAGIVT ALRSNGFYFQ DPNPDNNDAT SEAIFVFTSS
APTVAIGDSI LVNGKVSEFR PGNNANNLTT TEITSPSITK LSSGNALPTA TILGNGGRTI
PTSVIENDAT NVETSGIFDP AQDGIDFYES LEGMRVQINN AVSVSPTNNF GEIWVLSDNG
ANATGKTARG GIGLSANDFN PERIQIDPAL LTSGSTANLN LGTTFNTITG VVDYSFSNFE
VLPTSLSVAT PSTLQKEVTN LAPTANQLTV ATFNVENLDI GDGAAKFNAL ASQIVNNLKS
PDIINLQEIQ DNNGATNNGV VDASTTLQTL INAIAAAGGP TYQFRQVNPV DGTNGGEPGG
NIRPAFLFNP NRVSFVDIAG GTSTSNTTVT NVSGVPTLSA SSGLIDPTNS AFDSSRKPLV
GQFTFNGQSV YVIDNHFNSK GGDQPLYGPN QPPVLSSEVQ RNQQATIVKN FVRDILNVNP
NANVIVAGDL NDFSFSNPLN ILKSAGLTDL VSTLPANEQY DYVFEGNSQD LDHILASGNL
VNNLDGVDVV HVNSEFASQT SDHDPILARF NIASNLINGT PGRDTLIGTS GNDIITGYQG
ADTLTGGLGS DKFVFTSTKD GKDTITDFTS GADQIVLTSL FQSAGLSGLN YTNAISQGYL
SFGTSGNDTN VLIDLDGFAG SAFRSAPLVT VQKVNSTTLA SSSNFVF
//
